title: Crystallization and preliminary X-ray investigation of human erythrocytic purine nucleoside phosphorylase.
abstract: Crystals of human erythrocytic purine nucleoside phosphorylase have been grown from solutions of ammonium sulfate. The crystals are trigonal, space group R32; the hexagonal axes are a = 143.8(2) and c = 165.1(2) A. The crystals are moderately stable to x-rays and diffract beyond 3.0 A resolution. The experimental density of the crystals indicates that the molecular weight of the protein is 94,000. The three subunits are not related by crystallographic symmetry.
mesh_terms: D003460:Crystallization; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D008970:Molecular Weight; D010430:Pentosyltransferases / Q000097:blood*; D011487:Protein Conformation; D011683:Purine-Nucleoside Phosphorylase / Q000097:blood* / Q000302:isolation & purification; D014961:X-Ray Diffraction
chemical_list: D010430:Pentosyltransferases; D011683:Purine-Nucleoside Phosphorylase